Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
about
Developing Universal Influenza Vaccines: Hitting the Nail, Not Just on the HeadStructural characterization of viral epitopes recognized by broadly cross-reactive antibodiesInfluenza Human Monoclonal Antibody 1F1 Interacts with Three Major Antigenic Sites and Residues Mediating Human Receptor Specificity in H1N1 VirusesA recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutininAntibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding SiteA common solution to group 2 influenza virus neutralizationReceptor mimicry by antibody F045–092 facilitates universal binding to the H3 subtype of influenza virusAlternative Recognition of the Conserved Stem Epitope in Influenza A Virus Hemagglutinin by a VH3-30-Encoded Heterosubtypic AntibodyConserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza VirusesAnti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus BindingMax Bergmann lecture protein epitope mimetics in the age of structural vaccinologyModified vaccinia virus ankara (MVA) as production platform for vaccines against influenza and other viral respiratory diseasesInfluenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protectionLarge-scale analysis of B-cell epitopes on influenza virus hemagglutinin - implications for cross-reactivity of neutralizing antibodies.The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency.The Analysis of B-Cell Epitopes of Influenza Virus Hemagglutinin.Emerging antiviral strategies to interfere with influenza virus entry.Relating influenza virus membrane fusion kinetics to stoichiometry of neutralizing antibodies at the single-particle levelCombination of the immunization with the sequence close to the consensus sequence and two DNA prime plus one VLP boost generate H5 hemagglutinin specific broad neutralizing antibodies.A broadly neutralizing human monoclonal antibody directed against a novel conserved epitope on the influenza virus H3 hemagglutinin globular headCharacterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin.Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses.Influenza virus antigenicity and broadly neutralizing epitopes.Strategies to guide the antibody affinity maturation processComprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infectionRational Design of an Epstein-Barr Virus Vaccine Targeting the Receptor-Binding SiteHemagglutinin stalk-based universal vaccine constructs protect against group 2 influenza A viruses.Broadly neutralizing antibodies against influenza viruses.Development and applications of single-cycle infectious influenza A virus (sciIAV).Heads, stalks and everything else: how can antibodies eradicate influenza as a human disease?A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Increasing the breadth and potency of response to the seasonal influenza virus vaccine by immune complex immunization.From Original Antigenic Sin to the Universal Influenza Virus Vaccine.Heterosubtypic cross-reactivity of HA1 antibodies to influenza A, with emphasis on nonhuman subtypes (H5N1, H7N7, H9N2).Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site.In vitro evolution of an influenza broadly neutralizing antibody is modulated by hemagglutinin receptor specificity.Divergent Requirement of Fc-Fcγ Receptor Interactions for In Vivo Protection against Influenza Viruses by Two Pan-H5 Hemagglutinin Antibodies.In vivo dendritic cell targeting cellular vaccine induces CD4(+) Tfh cell-dependent antibody against influenza virus.Prospects of HA-based universal influenza vaccine.
P2860
Q26783897-3E9D0326-DAE5-4222-A700-EF3EEFDEEA0EQ26823492-88CD5FD1-DB16-424F-B3A3-DDE692708115Q27675477-287EC6DF-5272-4633-AF31-DC5B5DD5677DQ27676298-EDCB9813-80D5-4EE7-BDF0-E403DD64EEBFQ27679927-3E3847ED-0CA7-4F0F-967B-4A2535BC6520Q27680873-6EF5A543-DA36-4CEF-AD4D-18949448E66BQ27683156-3897191E-E837-49D5-9301-5C618C98BA1DQ27683187-EFBFD032-F5FA-4FAA-BFC2-A330C012C20BQ27683198-66F296E0-FFA2-472D-AA70-7CA8F42304CCQ28552622-594E6B1B-6837-45D9-A350-BE6CF366DDC6Q30155145-CD522BAC-922B-4D5F-BFE0-8036523E1B83Q30209342-0FDA00A2-DE44-46FA-8640-F953AF8AAAC4Q30209769-3BCBF702-5210-4D71-9148-F55C1550EAA0Q30217235-C85ECEB6-B5F2-41A5-9CE8-6FE27E2D6C51Q30365366-9D85B049-12A4-4E9A-84B3-AF615D7FC64AQ30387177-4E339A4E-9EA3-4FAF-83EA-1E4A68ECF62AQ30432421-E635E3EC-17EC-4428-8D81-367E2763BBA4Q30606286-2B1D922D-28A4-43BE-9022-F58AD7B21835Q33724743-341139E7-EE84-413D-985C-56AF358D81F4Q33743865-8697B557-07A7-4161-A194-85ABEF814ADCQ34594065-66371C67-4E66-4001-9217-0ABAA58C7D19Q35132253-B5121092-7341-43E5-B565-21EE91596CB8Q35685270-182F7F72-DA4A-414F-815F-E246155B250AQ35685300-34A0EA0F-B337-40C8-97AD-4A352E8DFF5CQ36392511-2DF3330A-590B-41AE-B38D-23CD784A1541Q36590540-8192975F-6241-4C5C-9A45-A60A8DC1C9CAQ37252968-28F06357-C844-4B84-A223-FFB06E18432EQ37704975-86331CF0-6543-4C93-B7AE-A35FC4AB8D19Q38556537-5CF4BF61-CB5C-4459-99DE-133D11CAFD3EQ38804059-CE40EBE1-D4F5-457B-93E8-FCA07CBCD1ADQ39397313-3F032E25-1DF0-41CA-AEE6-055045D6D9F1Q40056879-A4A19160-E11C-46BE-9EA4-19D9BDC12B26Q40059787-542D6568-6043-4C3F-93A1-5073D4F0AA99Q40120056-CC4FFCCF-6B57-422B-89C7-1F2935AE488DQ40158695-7CB3043C-AAE0-4DC6-B2B4-B615019446C9Q40163658-F9CF5E08-AC77-4E37-8C4C-85E3F5856CD9Q40201534-515A3A4C-AD87-490A-989F-2BC26C5819F5Q40279321-8C9FE488-FD8F-4E48-8203-9272BBCFE1E3Q40507213-0F71083E-BE85-41FA-8799-0155C7B5767BQ41416400-29D10698-407F-416D-9AAC-F9F11FEF0FED
P2860
Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@ast
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@en
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@nl
type
label
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@ast
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@en
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@nl
prefLabel
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@ast
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@en
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@nl
P2093
P2860
P3181
P356
P1476
Heterosubtypic antibody recogn ...... nding site enhanced by avidity
@en
P2093
Ayato Takada
Ian A Wilson
Peter S Lee
Reiko Yoshida
Yasuhiko Suzuki
P2860
P304
17040-17045
P3181
P356
10.1073/PNAS.1212371109
P407
P577
2012-10-01T00:00:00Z